Rat ventral prostate nucleus contains protein kinases which are sensitive to androgenic status of the animal. Phosphocellulose column chromatography has indicated the presence of multiple peaks of kinase activity. These are being purified further by utilizing affinity chromatography. In particular, attempt is being made to ascertain if multiple protein kinase activities are due to different molecular weights or due to differences in molecular net charges. Experiments are also proposed to further characterize protein kinase activities associated with human prostatic nuclei; activities towards acidic protein substrates and histones have been observed. Additional studies are designed to purify various kinases from human prostatic chromatin. Polyamines stimulate protein kinase reactions towards acidic protein substrates but not towards histones. These stimulatory effects are not due to nonspecific changes in the ionic strength or to substitution of spermine for Mg2 ion. Experiments are underway to examine the effects of polyamines on phosphorylation of various nonhistone proteins in the prostatic chromatin preparations from animals of varying androgenic status.